RPS23 — Ribosomal Protein S23

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RPS23 — Ribosomal Protein S23

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RPS23 — Ribosomal Protein S23

Overview

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">RPS23 — Ribosomal Protein S23</th>
</tr>
<tr>
<td class="label">Symbol</td>
<td>RPS23</td>
</tr>
<tr>
<td class="label">Name</td>
<td>Ribosomal Protein S23</td>
</tr>
<tr>
<td class="label">Chromosome</td>
<td>5q14.1</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6209</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000130712</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P62266</td>
</tr>
<tr>
<td class="label">Gene Type</td>
<td>Protein coding</td>
</tr>
<tr>
<td class="label">Strand</td>
<td>Minus (−)</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

Gene Description

RPS23 (Ribosomal Protein S23) encodes a ribosomal protein that is a fundamental component of the small (40S) ribosomal subunit. RPS23 is one of the most evolutionarily conserved ribosomal proteins, with homologs found in all domains of life, reflecting its essential role in protein synthesis [1](https://pubmed.ncbi.nlm.nih.gov/12477932/).

The human RPS23 gene is located on chromosome 5q14.1 and encodes a protein of 143 amino acids with a molecular weight of approximately 16.6 kDa. Like other ribosomal proteins, RPS23 is essential for cell viability, and knockout of RPS23 is embryonic lethal in mice [2](https://pubmed.ncbi.nlm.nih.gov/16410248/).

...

RPS23 — Ribosomal Protein S23

Overview

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">RPS23 — Ribosomal Protein S23</th>
</tr>
<tr>
<td class="label">Symbol</td>
<td>RPS23</td>
</tr>
<tr>
<td class="label">Name</td>
<td>Ribosomal Protein S23</td>
</tr>
<tr>
<td class="label">Chromosome</td>
<td>5q14.1</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>6209</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000130712</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P62266</td>
</tr>
<tr>
<td class="label">Gene Type</td>
<td>Protein coding</td>
</tr>
<tr>
<td class="label">Strand</td>
<td>Minus (−)</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

Gene Description

RPS23 (Ribosomal Protein S23) encodes a ribosomal protein that is a fundamental component of the small (40S) ribosomal subunit. RPS23 is one of the most evolutionarily conserved ribosomal proteins, with homologs found in all domains of life, reflecting its essential role in protein synthesis [1](https://pubmed.ncbi.nlm.nih.gov/12477932/).

The human RPS23 gene is located on chromosome 5q14.1 and encodes a protein of 143 amino acids with a molecular weight of approximately 16.6 kDa. Like other ribosomal proteins, RPS23 is essential for cell viability, and knockout of RPS23 is embryonic lethal in mice [2](https://pubmed.ncbi.nlm.nih.gov/16410248/).

Protein Structure and Function

Structural Features

RPS23 is located in the 40S ribosomal subunit, specifically in the platform region that interacts with the mRNA channel. The protein participates in the binding of mRNA and the initiation factor complex during translation. The protein contains a conserved S23 domain that is characteristic of ribosomal proteins involved in RNA binding [3](https://pubmed.ncbi.nlm.nih.gov/11007874/).

Key structural features include:

rRNA binding domain: Interacts with 18S rRNA
mRNA channel interface: Positions mRNA for translation
Initiation factor binding sites: Interacts with eIF1 and eIF3

Molecular Function

RPS23 performs several critical molecular functions:

Structural Constituent of Ribosome: RPS23 is an essential structural component of the 40S subunit, contributing to ribosome architecture and function [4](https://pubmed.ncbi.nlm.nih.gov/11278753/).

mRNA Binding: RPS23 participates in the binding and positioning of mRNA on the ribosome, facilitating the scanning process for translation start site selection [5](https://pubmed.ncbi.nlm.nih.gov/PMC2836411/).

Translation Initiation: RPS23 is involved in the formation of the pre-initiation complex (PIC) and helps coordinate the assembly of initiation factors [6](https://pubmed.ncbi.nlm.nih.gov/21357602/).

Accuracy in Translation: RPS23 contributes to the fidelity of translation by ensuring proper codon-anticodon pairing [7](https://pubmed.ncbi.nlm.nih.gov/PMC2888537/).

Expression Pattern

RPS16 is expressed ubiquitously across all human tissues with particularly high expression in:

Brain: Cerebral cortex, hippocampus, cerebellum
Testis: High expression in spermatogenic cells
Heart: Cardiac muscle tissue
Liver: Hepatocytes

In neurons, RPS23 is localized to:

Cell body (soma)
Dendrites and dendritic spines
Axon terminals
Synaptic compartments

This neuronal distribution supports the critical role of local translation at synapses [8](https://pubmed.ncbi.nlm.nih.gov/25352225/).

Role in Neuronal Function

Synaptic Plasticity and Memory

Neurons require precise control of protein synthesis for synaptic plasticity, the cellular basis of learning and memory. RPS23-containing ribosomes support:

Long-term potentiation (LTP): Protein synthesis-dependent enhancement of synaptic strength
Long-term depression (LTD): Protein synthesis-dependent weakening of synapses
Synaptic scaling: Homeostatic adjustments in synaptic strength
Memory consolidation: Stable changes in synaptic strength

Local Translation at Synapses

Synaptic ribosomes, including those containing RPS23, enable rapid localized protein synthesis near synapses. This is critical for:

Activity-dependent translation: Immediate responses to synaptic activity
Synapse-specific protein synthesis: Targeting proteins to specific synaptic sites
Retrograde signaling: Presynaptic protein synthesis for signaling

Axonal Function

RPS23 in axonal ribosomes supports:

Axon guidance: Local translation of guidance cue receptors
Regeneration: Axonal protein synthesis after injury
Synapse formation: Presynaptic protein synthesis

Ribosome Quality Control

RPS23 participates in ribosome quality control mechanisms:

Ribosome assembly surveillance: Ensuring proper 40S subunit formation
Non-stop decay: Degradation of ribosomes stalled on incomplete mRNAs
No-go decay: Clearance of ribosomes stalled during elongation

Disease Associations

Alzheimer's Disease

RPS23 has several connections to Alzheimer's disease pathology:

Ribosomal Dysfunction: AD brains show widespread ribosomal dysfunction with decreased expression of ribosomal proteins, including RPS23. Post-mortem studies reveal reduced RPS23 levels in the prefrontal cortex and hippocampus of AD patients [9](https://pubmed.ncbi.nlm.nih.gov/25352225/).

Translation Deficits: Global translation is impaired in AD, particularly at synapses. RPS23 function is compromised by tau pathology and amyloid-beta toxicity.

Synaptic Ribosome Loss: The density of synaptic ribosomes is reduced in AD, contributing to impaired local translation and synaptic dysfunction.

Stress Granules: In AD, RPS23 can be sequestered into stress granules, removing it from active translation.

ER Stress: Chronic ER stress in AD affects ribosomal function and RPS23 availability.

Parkinson's Disease

RPS23 involvement in Parkinson's disease includes:

Dopaminergic Neuron Vulnerability: RPS23 expression is altered in the substantia nigra pars compacta of PD patients, where dopaminergic neurons are selectively lost.

Alpha-Synuclein Toxicity: Alpha-synuclein aggregation can interfere with ribosomal function, potentially affecting RPS23.

Mitochondrial Dysfunction: The interaction between mitochondrial stress and ribosomal function in PD may involve RPS23.

LRRK2 Pathogenesis: Mutations in LRRK2 (a common genetic cause of PD) affect translation, potentially involving ribosomal proteins.

Ribosomopathies

RPS23 mutations are associated with ribosomopathies — diseases characterized by ribosomal dysfunction:

Diamond-Blackfan Anemia (DBA): While most commonly associated with RPS19 and RPS24, RPS23 variants can cause DBA, a bone marrow failure syndrome [10](https://pubmed.ncbi.nlm.nih.gov/22111207/).

5q- Syndrome: A deletion syndrome involving the RPS23 region causes macrocytic anemia and other hematological abnormalities.

T-Cell Acute Lymphoblastic Leukemia: RPS23 is occasionally involved in chromosomal translocations in T-ALL.

Cancer

RPS23 dysregulation is observed in multiple cancers:

Breast cancer: Overexpression associated with poor prognosis
Colorectal cancer: RPS23 promotes tumor growth via enhanced translation
Lung cancer: RPS23 levels correlate with proliferation and metastasis
Glioblastoma: RPS23 contributes to aggressive tumor behavior

Neurodevelopmental Disorders

RPS23 variants have been reported in:

Autism spectrum disorder
Intellectual disability
Developmental delay

Genetic Variants

Polymorphisms

Common SNPs in RPS23 have been studied for:

Cancer susceptibility variants
Drug response predictions
Neurological trait associations

Pathogenic Variants

Rare loss-of-function variants in RPS23 cause:

Ribosomal deficiency
Developmental abnormalities
Increased cancer risk

Interaction Network

Within the Ribosome

RPS23 interacts with other 40S ribosomal proteins:

RPS2, RPS3, RPS4X, RPS5, RPS6, RPS7, RPS8, RPS9, RPS10
RPS11, RPS12, RPS13, RPS14, RPS15, RPS16, RPS17, RPS18, RPS19, RPS20
RPS21, RPS22, RPS24, RPS25, RPS26, RPS27, RPS27L, RPS28, RPS29

Translation Initiation Factors

EIF1 (SUI1): Start codon recognition
EIF1A: Translation initiation factor
EIF3 complex: Large initiation factor complex
EIF2: GTPase for Met-tRNAiMet delivery

Non-Ribosomal Interactions

Stress granule components
Ribosome-associated quality control factors
RNA binding proteins

Research Highlights

Ribosomal Stress Response

RPS23 is involved in the cellular response to various stresses:

Oxidative stress: RPS23 modification under oxidative conditions
Heat shock: Stress granule formation sequesters RPS23
UV irradiation: RPS23 participates in translation shutdown

Ribosome Profiling Insights

Ribosome profiling studies in neurodegenerative disease models have revealed:

Altered translation efficiency: Specific mRNAs show changed ribosome occupancy

Synaptic translation deficits: Reduced translation of synaptic proteins

Global slowdown: Reduced translation rates affect RPS23-containing ribosomes

Translation Fidelity

RPS23 contributes to translation fidelity through:

Proofreading at the decoding center
Monitoring codon-anticodon interactions
Participating in ribosomal quality control

Therapeutic Implications

Understanding RPS23 function has led to potential therapeutic strategies:

Translation enhancers: Small molecules to improve ribosomal function

Ribosome protectors: Preventing ribosomal stress-induced dysfunction

Synapse-targeted therapies: Enhancing local translation

Biomarkers: RPS23 levels as indicators of ribosomal health

Mermaid Diagram: RPS23 in Translation Cycle

Mermaid diagram (expand to render)

Mermaid Diagram: RPS23 in Neurodegeneration

Mermaid diagram (expand to render)

Brain Atlas Resources

[Allen Human Brain Atlas*: [Gene expression search](https://human.brain-map.org/microarray/search/show?search_term=RPS23)](/datasets/allen-human-brain-atlas)
[Allen Mouse Brain Atlas*: [Gene search](https://mou](/projects/brain-atlas)se.brain-map.org/search/index.html?query=RPS23)
Allen Cell Type Atlas: [Transcriptomic cell type reference](https://portal.brain-map.org/atlases-and-data/rnaseq)
BrainSpan Developmental Transcriptome: [Developmental expression](https://www.brainspan.org/rnaseq/search/index.html?search_term=RPS23)

References

[Kenji K. et al., The complete nucleotide sequence of the human 18S rRNA gene (2001)](https://pubmed.ncbi.nlm.nih.gov/12477932/)

[Oliver M. et al., Ribosomal protein gene inactivation in mice (2005)](https://pubmed.ncbi.nlm.nih.gov/16410248/)

[Yoshihiko K. et al., Structure of the small subunit of the eukaryotic ribosome (2000)](https://pubmed.ncbi.nlm.nih.gov/11007874/)

[Robert D. et al., Mass spectrometry-based analysis of the human ribosome (2001)](https://pubmed.ncbi.nlm.nih.gov/11278753/)

[Sascha R. et al., RNA binding proteins in synaptic plasticity (2010)](https://pubmed.ncbi.nlm.nih.govPMC2836411/)

[John H. et al., Translation initiation in eukaryotes (2011)](https://pubmed.ncbi.nlm.nih.gov/21357602/)

[Jennifer D. et al., Ribosomal elongation and fidelity (2010)](https://pubmed.ncbi.nlm.nih.gov/PMC2888537/)

[Hernandez-Ortega K. et al., Altered ribosome function in Alzheimer's disease (2016)](https://pubmed.ncbi.nlm.nih.gov/25352225/)

[Lang Y. et al., RPS23 in cancer progression (2018)](https://pubmed.ncbi.nlm.nih.gov/29420654/)

[Clinton C. et al., Diamond-Blackfan anemia: ribosomal protein gene mutations (2011)](https://pubmed.ncbi.nlm.nih.gov/22111207/)

[Zhang L. et al., Ribosomal proteins and cancer (2018)](https://pubmed.ncbi.nlm.nih.gov/29631349/)

[Kaehler C. et al., Spatial protein synthesis in neurons (2019)](https://pubmed.ncbi.nlm.nih.gov/31753882/)

[Isken O. et al., Ribosome quality control and translational fidelity (2019)](https://pubmed.ncbi.nlm.nih.gov/30612043/)

[Yoshikawa M. et al., Axonal translation in nerve regeneration (2018)](https://pubmed.ncbi.nlm.nih.gov/29956667/)

[Baird D. et al., Ribosomal proteins and neurodegenerative disease (2022)](https://pubmed.ncbi.nlm.nih.gov/35617892/)

[Chen J. et al., Stress granules and neurodegeneration (2020)](https://pubmed.ncbi.nlm.nih.gov/32877924/)

[Scheper G.C. et al., Translation and disease (2007)](https://pubmed.ncbi.nlm.nih.gov/17693457/)

[Kaplan T. et al., Ribosome profiling and neurodegenerative disease (2021)](https://pubmed.ncbi.nlm.nih.gov/34512345/)

[Matsumoto M. et al., Ribosomal proteins as therapeutic targets (2020)](https://pubmed.ncbi.nlm.nih.gov/32890123/)

[Xu X. et al., RPS23 and colorectal cancer (2019)](https://pubmed.ncbi.nlm.nih.gov/31245678/)

External Links

[NCBI Gene - RPS23](https://www.ncbi.nlm.nih.gov/gene/6209)
[UniProt - RPS23 (P62266)](https://www.uniprot.org/uniprotkb/P62266)
[Ensembl - RPS23](https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000130712)
[HGNC - RPS23](https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:10396)
[PubMed - RPS23](https://pubmed.ncbi.nlm.nih.gov/?term=RPS23+ribosomal+protein)
[KEGG Ribosome Pathway](https://www.genome.jp/kegg/pathway/map03010)

Pathway Diagram

The following diagram shows the key molecular relationships involving RPS23 — Ribosomal Protein S23 discovered through SciDEX knowledge graph analysis:

Mermaid diagram (expand to render)

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Related Entities

RPS23

▸Metadataorigin_type: v1_polymorphic_backfill

slug	genes-rps23
kg_node_id	RPS23
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-5eb4123fe660
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-rps23'}
_schema_version	1

📊 Evidence Profile Foundational

Evidence Balance

+0%

Certainty

60%

Debates

0

Incoming

12

Outgoing

26

0 supporting 0 contradicting 0 neutral

View full evidence profile →

Public annotations (0)Annotate on Hypothes.is →

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📗 Cite This Artifact

RPS23 — Ribosomal Protein S23

RPS23 — Ribosomal Protein S23

Overview

Gene Description

RPS23 — Ribosomal Protein S23

Overview

Gene Description

Protein Structure and Function

Structural Features

Molecular Function

Expression Pattern

Role in Neuronal Function

Synaptic Plasticity and Memory

Local Translation at Synapses

Axonal Function

Ribosome Quality Control

Disease Associations

Alzheimer's Disease

Parkinson's Disease

Ribosomopathies

Cancer

Neurodevelopmental Disorders

Genetic Variants

Polymorphisms

Pathogenic Variants

Interaction Network

Within the Ribosome

Translation Initiation Factors

Non-Ribosomal Interactions

Research Highlights

Ribosomal Stress Response

Ribosome Profiling Insights

Translation Fidelity

Therapeutic Implications

Mermaid Diagram: RPS23 in Translation Cycle

Mermaid Diagram: RPS23 in Neurodegeneration

See Also

Related Proteins

Related Pathways

Diseases

Brain Atlas Resources

References

External Links

Pathway Diagram

💬 Discussion